Date Approved
2022
Degree Type
Open Access Senior Honors Thesis
Department or School
Chemistry
First Advisor
Brittany Albaugh, Ph.D.
Second Advisor
Hedeel Evans, Ph.D.
Third Advisor
Deborah Heyl-Clegg, Ph.D.
Abstract
Epigenetics is the study of regulating gene expression without changing the DNA sequence. Ubiquitin-like containing Plant Homeodomain and Ring-Finger 2 (UHRF2) is an epigenetic protein that is both overexpressed and underexpressed in various types of cancers. Recent studies have shown the Tandem Tudor Domain (TTD) and Planthomeo Domain (PHD) of UHRF2 interact with histone 3 trimethylated at lysine 9 (H3K9me3). However, the structural basis for UHRF2 TTD-PHD binding H3K9me3 has not been determined. This project consists of purification of the UHRF2 TTD-PHD protein construct expressed in E. coli, crystallization of the protein, X-ray diffraction of the crystal, and molecular replacement and refinement in order to generate the crystal structure of UHRF2 TTD-PHD with H3K9me3. This protein structure will provide critical insights into the molecular mechanism of histone binding by UHRF2, which can eventually be used to specifically target UHRF2 in cancer as a long-term goal.
Recommended Citation
Miller, Isaak, "X-ray crystallography of protein UHRF2 with H3K9me3" (2022). Senior Honors Theses and Projects. 744.
https://commons.emich.edu/honors/744